ATP-driven remodeling of the linker domain in the dynein motor

Structure. 2012 Oct 10;20(10):1670-80. doi: 10.1016/j.str.2012.07.003. Epub 2012 Aug 2.


Dynein ATPases are the largest known cytoskeletal motors and perform critical functions in cells: carrying cargo along microtubules in the cytoplasm and powering flagellar beating. Dyneins are members of the AAA+ superfamily of ring-shaped enzymes, but how they harness this architecture to produce movement is poorly understood. Here, we have used cryo-EM to determine 3D maps of native flagellar dynein-c and a cytoplasmic dynein motor domain in different nucleotide states. The structures show key sites of conformational change within the AAA+ ring and a large rearrangement of the "linker" domain, involving a hinge near its middle. Analysis of a mutant in which the linker "undocks" from the ring indicates that linker remodeling requires energy that is supplied by interactions with the AAA+ modules. Fitting the dynein-c structures into flagellar tomograms suggests how this mechanism could drive sliding between microtubules, and also has implications for cytoplasmic cargo transport.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Adenosine Diphosphate / chemistry
  • Adenosine Triphosphate / chemistry*
  • Axonemal Dyneins / chemistry*
  • Axonemal Dyneins / ultrastructure
  • Axoneme / ultrastructure
  • Chlamydomonas reinhardtii / enzymology*
  • Cryoelectron Microscopy
  • Dictyostelium / enzymology*
  • Microscopy, Video
  • Microtubules / chemistry
  • Microtubules / ultrastructure
  • Models, Molecular
  • Plant Proteins / chemistry
  • Plant Proteins / ultrastructure
  • Protein Binding
  • Protein Structure, Quaternary
  • Protein Structure, Tertiary
  • Protozoan Proteins / chemistry
  • Protozoan Proteins / ultrastructure
  • Structural Homology, Protein


  • Plant Proteins
  • Protozoan Proteins
  • Adenosine Diphosphate
  • Adenosine Triphosphate
  • Axonemal Dyneins